Q8C0M9 (ASGL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
L-asparaginase
EC=3.5.1.1

Alternative name(s):
Asparaginase-like protein 1
L-asparagine amidohydrolase

Gene names

Name:

Asrgl1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	326 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in asparagine catabolism. May be involved in astroglial production of L-aspartate, which can act as an excitatory neurotransmitter in some brain regions By similarity.
Catalytic activity	L-asparagine + H2O = L-aspartate + NH3.
Subcellular location	Cytoplasm By similarity. Note: Midpiece of sperm tail By similarity.
Sequence similarities	Belongs to the Ntn-hydrolase family.
Sequence caution	The sequence AAH16106.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB24431.1 differs from that shown. Reason: Frameshift at position 29. The sequence BAC25294.1 differs from that shown. Reason: Frameshift at positions 24 and 29.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	asparagine catabolic process via L-aspartate Inferred from sequence or structural similarity. Source: UniProtKB protein maturation Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 326	326	L-asparaginase		PRO_0000305206
Sites
	Active site	185	1	Nucleophile By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8C0M9 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: B5AC25922D9A1338	FASTA	326	33,950
	10 20 30 40 50 60 MACARGTVAP PVRASIDVSL VVVVHGGGAS NISANRKELV REGIARAATE GYKILKAGGS 70 80 90 100 110 120 AVDAVEGAVT VLENDPEFNA GYGSVLNVNG DIEMDASIMD GKDLSAGAVS AVRCIANPVK 130 140 150 160 170 180 LARLVMEKTP HCFLTGHGAE KFAEDMGIPQ VPVEKLITER TKKHLEKEKL EKGAQNADCP 190 200 210 220 230 240 KNSGTVGAVA LDCRGNLAYA TSTGGIVNKM VGRVGDSPCI GAGGYADNNL GAVSTTGHGE 250 260 270 280 290 300 SILKVNLARL ALFHVEQGKT VEEAAQLALD YMKSKLKGLG GLILVNKTGD WVAKWTSASM 310 320 PWAAVKNGKL QAGIDLCETR TRDLPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Testis.
[2]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-13; 103-120 AND 129-155, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-326. Strain: FVB/N. Tissue: Salivary gland.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK006147 mRNA. Translation: BAB24431.1. Frameshift. AK010381 mRNA. Translation: BAC25294.1. Frameshift. AK030209 mRNA. Translation: BAC26844.1. BC016106 mRNA. Translation: AAH16106.1. Different initiation.
IPI	IPI00223875.
RefSeq	NP_079886.2. NM_025610.3.
UniGene	Mm.272847.
3D structure databases
HSSP	HSSP built from PDB template 1K2X based on UniProtKB P37595.
ProteinModelPortal	Q8C0M9.
SMR	Q8C0M9. Positions 19-317.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8C0M9. 1 interaction.
STRING	Q8C0M9.
Protein family/group databases
MEROPS	T02.002.
2D gel databases
REPRODUCTION-2DPAGE	IPI00223875.
Proteomic databases
PRIDE	Q8C0M9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000049948; ENSMUSP00000051709; ENSMUSG00000024654.
GeneID	66514.
KEGG	mmu:66514.
UCSC	uc008gon.1. mouse.
Organism-specific databases
CTD	80150.
MGI	MGI:1913764. Asrgl1.
Phylogenomic databases
eggNOG	roNOG10540.
GeneTree	ENSGT00530000063034.
HOVERGEN	HBG101662.
OrthoDB	EOG4ZS93Q.
PhylomeDB	Q8C0M9.
Gene expression databases
ArrayExpress	Q8C0M9.
Bgee	Q8C0M9.
CleanEx	MM_ASRGL1.
Genevestigator	Q8C0M9.
Family and domain databases
InterPro	IPR000246. Peptidase_T2. [Graphical view]
KO	K13051.
PANTHER	PTHR10188. Peptidase_T2. 1 hit.
Pfam	PF01112. Asparaginase_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	321912.
SOURCE	Search...

Entry information

Entry name

ASGL1_MOUSE

Accession

Primary (citable) accession number: Q8C0M9
Secondary accession number(s): Q91WC8, Q9CVX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program